Our group uses Fourier transform mass spectrometry to characterize glycosaminoglycans (GAGs). GAGs are linear carbohydrates that play important roles in biological processes such as cell signaling, cellular communication and the regulation of biochemical pathways. GAGs are composed of repeating disaccharide units of an N-acetyl amino sugar and an uronic acid. Our group focuses on two families of GAGs, heparan sulfate (HS)/ heparin (Hp) and chondroitin sulfate (CS)/ dermatan sulfate (DS). These GAGs have chains that can be modified by deacetylases, sulfotransferases and epimerases, which produce highly complex structures. Our research aims to characterize complex GAG samples using tandem mass spectrometry (MS/MS). By using different threshold and electron based activation methods we are able to determine the position of sulfo modifications as well as C-5 uronic acid stereochemistry of GAG samples. Visit our "Research" section tabs to get a closer look at the research being done in our lab. Figure: Ly, M.; Leach III, F. E.; Laremore, T. N.; Toida, T; Amster, I. J.; Linhardt, R. J. “The Proteogylcan Bikunin Has a Defined Sequence”, Nature Chem. Biol.2011, 7, 827-833.
